INTERACTIONS OF APOLIPOPROTEIN A-I N- AND C-TERMINI

载脂蛋白 A-I N 端和 C 端的相互作用

• 批准号: 7723035
• 负责人: DAVID ATKINSON
• 金额: $ 0.13万
• 依托单位: BOSTON UNIVERSITY MEDICAL CAMPUS
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-06-01 至 2009-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7723035
• 关键词: Apolipoprotein A-I; Atherosclerosis; Back; C-terminal; Cholesterol; Computer Retrieval of Information on Scientific Projects Database; Data; Funding; Grant; Hepatic Tissue; High Density Lipoproteins; Human; Institution; Lipid Binding; Lipids; Literature; Liver; Manuscripts; Mass Spectrum Analysis; Modeling; Molecular Conformation; N-terminal; Peptides; Phospholipids; Play; Pliability; Proteins; Research; Research Personnel; Resources; Role; Source; Structure; Techniques; United States National Institutes of Health; Work; apolipoprotein Lp(a+)

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Previous work in our lab and data in the literature have consistently suggested that the Human apolipoprotein A-I (ApoA-I), is the principal protein component of high-density lipoprotein (HDL), which has a major function in transferring cholesterol from non-hepatic tissues back to the liver and thus plays a critical role in protection against atherosclerosis. The intrinsic flexibility of apoA-I allows its structure to adapt multiple conformations on different species of HDL that contain different amounts of phospholipids and cholesterol. Previous studies from our work and that of others has suggested the close proximity and thus the interaction between the N- and C-termini of ApoA-I in lipid- free conformation. The conformation and interaction of two peptide models, representing the N-terminal (residues 1-44) and C-terminal (residues 198-243) of apoA-I, have been investigated in lipid- free and lipid- bound forms by mass spectrometry and other methods. A manuscript describing our results is being prepared..

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 我们实验室的前期工作和文献数据一致表明，人载脂蛋白A-I（ApoA-I）是高密度脂蛋白（HDL）的主要蛋白组分，其主要功能是将胆固醇从非肝组织转移回肝脏，从而在预防动脉粥样硬化中起关键作用。apoA-I的内在灵活性允许其结构适应含有不同量的磷脂和胆固醇的不同种类的HDL的多种构象。来自我们工作的先前研究和其他人的研究已经表明ApoA-I在无脂质构象中的N-和C-末端之间的紧密接近和因此的相互作用。用质谱和其它方法研究了apoA-I的N-末端（残基1 - 44）和C-末端（残基198 - 243）的两种肽模型在无脂和脂结合形式下的构象和相互作用。一份描述我们结果的手稿正在准备中。